Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Boglárka H. Várkuti"'
Autor:
Máté Gyimesi, Gábor Szegvári, György Hegyi, Miklós Képiró, István Lőrincz, András Málnási-Csizmadia, Boglárka H. Várkuti, Mihály Kovács, Ádám I. Horváth
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Subcellular dynamics of non-muscle myosin 2 (NM2) is crucial for a broad-array of cellular functions. To unveil mechanisms of NM2 pharmacological control, we determined how the dynamics of NM2 diffusion is affected by NM2′s allosteric inhibitors, i
Autor:
Ze Liu, Miklós Képiró, Ronald L. Davis, Boglárka H. Várkuti, Theodore M. Kamenecka, Yunchao Gai, Rodrigo Pacifico
Publikováno v:
iScience
iScience, Vol 23, Iss 8, Pp 101364-(2020)
iScience, Vol 23, Iss 3, Pp-(2020)
iScience, Vol 23, Iss 8, Pp 101364-(2020)
iScience, Vol 23, Iss 3, Pp-(2020)
Summary We developed a high-throughput assay for modulators of mitochondrial function in neurons measuring inner mitochondrial membrane potential (ΔΨm) and ATP production. The assay was used to screen a library of small molecules, which led to the
Autor:
Ronald L. Davis, Boglárka H. Várkuti, Miklós Képiró, Kyle Vick, Rodrigo Pacifico, Theodore M. Kamenecka, Yosef Avchalumov, Courtney M. MacMullen, Sathyanarayanan V. Puthanveettil, Ze Liu
Publikováno v:
Science Advances
We have identified small molecules that potentiate aspects of mitochondrial dynamics and function in primary neurons.
Impaired mitochondrial dynamics and function are hallmarks of many neurological and psychiatric disorders, but direct screens f
Impaired mitochondrial dynamics and function are hallmarks of many neurological and psychiatric disorders, but direct screens f
High content, phenotypic screens offer a powerful approach to systems biology at the cellular level. The approach employs cells carrying fluorescently labeled molecules or organelles in 384- or 1536-well microplates, and an automated confocal screeni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a289a2448bebabdadc37fc2276dc667c
https://europepmc.org/articles/PMC6532062/
https://europepmc.org/articles/PMC6532062/
Autor:
Máté Varga, András Málnási-Csizmadia, István Ádám Horváth, Zsolt Lenkei, Boglárka H. Várkuti, Áron Zsigmond, László Végner, Miklós Képiró, György Hegyi, Szilvia Ráti
Publikováno v:
Scientific Reports
Blebbistatin is a commonly used molecular tool for the specific inhibition of various myosin II isoforms both in vitro and in vivo. Despite its popularity, the use of blebbistatin is hindered by its poor water-solubility (below 10 micromolar in aqueo
Autor:
Irén Bárdos-Nagy, Péter Erdélyi, Péter Hári, Boglárka H. Várkuti, Zhenhui Yang, András Málnási-Csizmadia, Attila L. Kovács, Tibor Vellai, Bálint Kintses, Miklós S.Z. Kellermayer
Publikováno v:
Nature Structural & Molecular Biology
F-actin serves as a track for myosin's motor functions and activates its ATPase activity by several orders of magnitude, enabling actomyosin to produce effective force against load. Although actin activation is a ubiquitous property of all myosin iso
Autor:
Máté Varga, Miklós Képiró, András Málnási-Csizmadia, Ádám I. Horváth, György Hegyi, Anna Á. Rauscher, Boglárka H. Várkuti, László Végner, Zsolt Borhegyi, Sharad Kumar, Zsolt Lenkei
Publikováno v:
Biophysical Journal. 112:266a-267a
Autor:
László Végner, Ádám I. Horváth, Szilvia Ráti, Boglárka H. Várkuti, Anna Á. Rauscher, Malnasi-Csizmadia Andras, Áron Zsigmond, Miklós Képiró, Máté Varga, Miklós S.Z. Kellermayer, Vanda Imrich
Publikováno v:
Biophysical Journal. 112:149a-150a
Autor:
Ádám I. Horváth, András Málnási-Csizmadia, György Hegyi, Miklós Képiró, Mihály Kovács, Boglárka H. Várkuti
Publikováno v:
Biophysical Journal. 112:430a
The cellular distribution of the motor protein non-muscle myosin 2 (NM2) leads to different forms of intracellular strain driving cell motility, cytokinesis and morphogenetic processes including axonal growth and retraction. However, it remains elusi
Publikováno v:
Journal of Biological Chemistry
We present the first in silico model of the weak−binding actomyosin in the initial powerstroke state, representing the actin-binding induced major structural changes in myosin. First, we docked an actin trimer to prepowerstroke myosin then relaxed